Molecular evolution of the aldo-keto reductase gene superfamily.
The aldo-keto reductase enzymes comprise a functionally diverse gene family which catalyze the NADPH-dependant reduction of a variety of carbonyl compounds. The protein sequences of 45 members of this family were aligned and phylogenetic trees were deduced from this alignment using the neighbor-joining and Fitch algorithms. The branching order of these trees indicates that the vertebrate enzymes cluster in three groups, which have a monophyletic origin distinct from the bacterial, plant, and invertebrate enzymes. A high level of conservation was observed between the vertebrate hydroxysteroid dehydrogenase enzymes, prostaglandin F synthase, and rho-crystallin of Xenopus laevis. We infer from the phylogenetic analysis that prostaglandin F synthase may represent a recent recruit to the eicosanoid biosynthetic pathway from the hydroxysteroid dehydrogenase pathway and furthermore that, in the context of gene recruitment, Xenopus laevis rho-crystallin may represent a shared gene.
Seery
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Center for Experimental Therapeutics, 905 Stellar Chance Laboratories, University of Pennsylvania, 422 Curie Boulevard, Philadelphia, PA 19103, USA.
Nestor
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FitzGerald
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D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D019143:Evolution, Molecular; D010802:Phylogeny; D016415:Sequence Alignment
D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase